The goal of this project is to study herpes simplex virus (HSV)-cell interaction and to provide the reagents for the study of HSV glycoprotein function and their expression on HSV-infected and -transformed cells. HSV has 5 major glycoproteins, A, B2, C2, D2, E, which can be distinguished by their molecular weights. The HSV glycoproteins determine the social behavior of the virus, are required for virus-cell recognition and binding, aid in HSV-induced syncytia formation and are responsible for the host immune recognition of HSV-infected cells. Procedures for the purification of the individual undenatured Herpes Simplex Virus (HSV) glycoproteins will be developed, monospecific and monoclonal antibodies to the individual glycoproteins will be prepared and used in the examination of HSV recognition and binding to target cells. The purification of non-ionic detergent-solubilized HSV glycoproteins will be facilitated by lectin affinity chromatography. Monospecific antisera will be prepared in rabbits to the individual purified glycoproteins and monoclonal antiodies prepared by fusion of spleen cells from immunized mice with the NS1 myeloma cell line. Monoclonal antibody production will provide large quantities of high titred, monospecific sera to each of the HSV glycoproteins allowing purification of large quantities of these glycoproteins by immunoaffinity methods, a first step in the production of a potential vaccine, and will be used as a specific neutralizing sera to block virus infection thereby defining the glycoprotein responsible. The virus recognition and binding phenomena will be further studied by direct binding of radioactively labelled HSV glycoproteins with the cell and by competition binding studies between the individual purified glycoproteins and virus. These studies will provide information as to the nature of the virus-viral receptor interaction.